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Receptor Tyrosine Kinases

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The mammalian target of rapamycin  (mTOR) is a serine/threonine kinase that regulates growth, proliferation, and cell survival in response to hormones, growth factors, or nutrient availability. This kinase exists in two structurally and functionally distinct forms: mTOR complex 1  (mTORC1) and mTOR complex 2  (mTORC2). The first form (mTORC1) is composed of a rapamycin-sensitive Raptor and proline-rich Akt substrate, PRAS40. In contrast,  mTORC2 consists of a...
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Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
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The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
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Several cytokine receptors have tightly bound Janus kinase or JAK proteins attached at their cytosolic tail. Small signaling molecules such as cytokines, growth hormones, or prolactins bind to the cytokine receptors and initiate their dimerization. The dimerization brings the cytosolic JAKs together that trans-phosphorylate and activates each other. The activated JAKs now phosphorylate cytosolic tails of the cytokine receptors, which serve as binding sites for adaptor proteins such as  SH2...
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Assessing Cellular Target Engagement by SHP2 PTPN11 Phosphatase Inhibitors
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Phosphatase PP2A promotes RTA dephosphorylation to impair KSHV lytic replication.

Lei Bai1, Lianghui Dong1, Jiazhen Dong1

  • 1State Key Laboratory of Virology and Biosafety, College of Life Sciences, Wuhan University, Wuhan, China.

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Summary

Kaposi

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Area of Science:

  • Virology
  • Molecular Biology
  • Biochemistry

Background:

  • Kaposi's Sarcoma-associated herpesvirus (KSHV) regulates latency and lytic replication via the RTA protein.
  • RTA phosphorylation is crucial for its function, but its regulation is not fully understood.

Purpose of the Study:

  • To investigate the role of RTA phosphorylation and dephosphorylation in KSHV lytic replication.
  • To identify host factors interacting with RTA and modulating its activity.

Main Methods:

  • Co-immunoprecipitation to identify RTA interacting proteins.
  • Western blotting to assess protein phosphorylation.
  • Viral replication assays to quantify progeny virions.
  • Ubiquitin-proteasome pathway analysis.

Main Results:

  • RTA interacts with PPP2R1A, a scaffold protein of phosphatase PP2A.
  • PPP2R1A and PP2A activation suppress KSHV lytic replication by dephosphorylating RTA.
  • KSHV RTA promotes PPP2R1A degradation via the ubiquitin-proteasome pathway to evade host control.

Conclusions:

  • PPP2R1A is a novel binding partner of RTA, mediating RTA dephosphorylation by PP2A.
  • This interaction suppresses KSHV lytic replication, offering potential antiviral targets.
  • KSHV RTA employs a counter-strategy by degrading PPP2R1A.